the results do not exclude the possibility that the HERV-K PR could complement an HIV-1 PR whoses function is impaired due to drugs or drug-resistant mutations, they clearly demomstrate that the HERV-K PR cannot substitute for the function of the wild-type HIV-1 PR

the N-terminal cleavage site for HERV-K capsid protein matches the sequence consistently found at the N-terminus of all retroviral capsid proteins. The other cleavage sites correspond well to the simplified version of a cleavage site as an amino acid stretch that is hydrophobic and both accessible and flexible, i.e. apparently the space between separately folded domainsof Gag

the results do not exclude the possibility that the HERV-K PR could complement an HIV-1 PR whoses function is impaired due to drugs or drug-resistant mutations, they clearly demomstrate that the HERV-K PR cannot substitute for the function of the wild-type HIV-1 PR

the enzyme is synthesized as monomeric part of the Gag polyprotein or the Gag-Pol polyprotein and autolytically processed to the mature protein dimer, autoprocessing at the N-terminal sequence Lys-Ala-Ala-Tyr-Trp-Ala-Ser-Gln

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Cloned/COMMENTARY

ORGANISM

UNIPROT

LITERATURE

213 amino acids of the 3'-end of the HERV-K protease open reading frame are expressed in Escherichia coli. Autocatalytic cleavage of the expressed polypeptide results in a catalytically active 18200 Da protein

targeting of the HERV-K PR to protease-deficient HIV-1 virions by expressing it as a Vpr fusion partner. The Vpr fusion proteins are sucessfully delivered to the HIV-1 virions, where the HERV-K PR not only autoprocesses itself to ist mature form, but also cleaves a number of HIV-1 polyproteins

the HERV-K113 sequence is cloned into a small plasmid vector. It is shown that based on a substantial LTR-promoter activity, full length messenger RNA and spliced env-, rec- and 1.5 kb (hel)-transcripts are produced. Envelope protein of HERV-K113 is synthesized as an 85 kDa precursor that is found partially processed. The accessory Rec protein is highly expressed and accumulates in the nucleus. Expression analysis reveals synthesis of the Gag precursor and the protease in lysates of transfected HEK-293T cells. The cloned HERV-K113 provirus is not replication competent

in the present study HIV-1 and HCV-1-positive plasma samples are screened for the presence of HERV-K(HML-2) RNA in an RT-PCR using HERV-K pol specific primers. Type 1 and type 2 HERV-K(HML- 2) viral RNA genomes are found to coexist in the same plasma of HIV-1 patients suggesting that HERV-K(HML-2) viral particles are induced in HIV-1-infected individuals